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J. Biol. Chem., Vol. 276, Issue 36, 33645-33651, September 7, 2001
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From the Botanisches Institut der
Ludwig-Maximilians-Universität, Menzingerstrasse 67, D-80638 München, Germany
A new component of the chloroplast proteolytic
machinery from Arabidopsis thaliana was identified as a
SppA-type protease. The sequence of the mature protein, deduced from a
full-length cDNA, displays 22% identity to the serine-type
protease IV (SppA) from Escherichia coli and 27% identity
to Synechocystis SppA1 (sll1703) but lacks the
putative transmembrane spanning segments predicted from the E. coli sequence. The N-terminal sequence exhibits typical features
of a cleavable chloroplast stroma-targeting sequence. The chloroplast
localization of SppA was confirmed by in organello import
experiments using an in vitro expression system and by immunodetection with antigen-specific antisera. Subfractionation of
intact chloroplasts demonstrated that SppA is associated exclusively with thylakoid membranes, predominantly stroma lamellae, and is a part
of some high molecular mass complex of about 270 kDa that exhibits proteolytic activity. Treatments with chaotropic salts and
proteases showed that SppA is largely exposed to the stroma but that it
behaves as an intrinsic membrane protein that may have an unusual
monotopic arrangement in the thylakoids. We demonstrate that SppA is a
light-inducible protease and discuss its possible involvement in the
light-dependent degradation of antenna and photosystem II
complexes that both involve serine-type proteases.
Identification and Characterization of SppA, a Novel
Light-inducible Chloroplast Protease Complex Associated with
Thylakoid Membranes*
*
This work was supported by Deutsche Forschungsgemeinschaft
Grant DFG SO448/2-1 (to A. S.) and SFB 184 (to R. H.) and the
Fonds der Chemischen Industrie.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
49-89-17861242; Fax: 49-89-1782274; E-mail:
anna@botanik.biologie.uni-muenchen.d.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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